Species: Rhodovulum sulfidophilum
Subunit composition of
dimethylsulfide dehydrogenase = [DdhA][DdhB][DdhC]
dimethylsulfide dehydrogenase α subunit = DdhA
dimethylsulfide dehydrogenase β subunit = DdhB (summary available)
dimethylsulfide dehydrogenase γ subunit = DdhC
Dimethylsulfide dehydrogenase catalyzes the oxidation of dimethyl sulfide to dimethyl sulfoxide (DMSO) during photoautotrophic growth of the purple non-sulfur phototrophic bacterium Rhodovulum sulfidophilum.
The enzyme was purified to homogeneity and found to be a complex of 152 kDa, composed of three distinct subunits [Hanlon96]. The enzyme can reduce a variety of N-oxides using reduced methylviologen as electron donor but dimethyl sulfoxide is reduced at a very low rate. The enzyme contains a cytochrome with a b-type heme and a guanylyl molybdenum cofactor cofactor, as well as multiple iron-sulfur clusters [McDevitt02]. The heme and pterin molybdenum cofactor are associated with the 94-kDa subunit.
Analysis of a ddhA mutant showed that dimethylsulfide dehydrogenase was essential for photolithotrophic growth of the organism on dimethyl sulfide but not for chemotrophic growth on the same substrate. Mutational analysis showed that cytochrome c2 mediated photosynthetic electron transfer from the enzyme to the photochemical reaction centre, although this cytochrome was not essential for photoheterotrophic growth of the bacterium [McDevitt02].
Molecular Weight: 152.0 kD (experimental) [Hanlon96]
Enzymatic reaction of: dimethylsulfide dehydrogenase
Synonyms: dimethylsulfide:receptor oxidoreductase
EC Number: 188.8.131.52dimethyl sulfide + 2 an oxidized cytochrome c2 + H2O → dimethyl sulfoxide + 2 a reduced cytochrome c2 + 2 H+
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: dimethyl sulfide degradation III (oxidation)
|Gene:||ddhA||Accession Number: G-10873 (MetaCyc)|
Molecular Weight: 102.31 kD (from nucleotide sequence)
Molecular Weight: 94.0 kD (experimental)
Relationship Links: InterPro:IN-FAMILY:IPR006311, InterPro:IN-FAMILY:IPR006655, InterPro:IN-FAMILY:IPR006656, InterPro:IN-FAMILY:IPR006657, InterPro:IN-FAMILY:IPR006963, InterPro:IN-FAMILY:IPR009010, InterPro:IN-FAMILY:IPR017840, Pfam:IN-FAMILY:PF00384, Pfam:IN-FAMILY:PF01568, Prosite:IN-FAMILY:PS00932, Prosite:IN-FAMILY:PS51318, Prosite:IN-FAMILY:PS51669
|Gene:||ddhB||Accession Number: G-10874 (MetaCyc)|
Molecular Weight: 37.026 kD (from nucleotide sequence)
Molecular Weight: 38.0 kD (experimental) [Hanlon96]
The DdhB subunit contains four putative [Fe-S] clusters [McDevitt02]
|Gene:||ddhC||Accession Number: G-10875 (MetaCyc)|
Molecular Weight: 29.499 kD (from nucleotide sequence)
Molecular Weight: 32.0 kD (experimental) [Hanlon96]
Unification Links: UniProt:Q8GPG1
Hanlon96: Hanlon SP, Toh TH, Solomon PS, Holt RA, McEwan AG (1996). "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor." Eur J Biochem 239(2);391-6. PMID: 8706745
McDevitt02: McDevitt CA, Hugenholtz P, Hanson GR, McEwan AG (2002). "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes." Mol Microbiol 44(6);1575-87. PMID: 12067345
Park06: Park YJ, Yoo CB, Choi SY, Lee HB (2006). "Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1." J Biochem Mol Biol 39(1);46-54. PMID: 16466637
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